Abstract
In this assay we used polystyrene-tube-attached rabbit antibodies against prostatic acid phosphatase (PAP) that had been purified to homogeneity from human prostate. The amount of immunoreactive acid phosphatase was determined directly by its enzymic activity in the solid-phase-bound immune complex. The detection limit was 0.05 U/L (0.13 microgram/L), the CVs between 4.3 and 10.8%. Investigating the organ specificity of PAP, we found that some cross-reacting acid phosphatase activity could be so measured in human kidney, leukocytes, and platelets, all of which probably contribute to the circulating "prostatic" acid phosphatase that normally is present in serum. Diurnal and day-to-day variations in serum PAP activity were as much as 100% in healthy subjects. Individuals without prostatic diseases (n = 92) had values for serum PAP activity up to 0.36 U/L (0.94 microgram/L), in an age-independent distribution; patients with benign prostatic hyperplasia (n = 62) showed values up to 0.48 U/L (1.25 micrograms/L). With PAP activity of 0.38 U/L or 1.0 microgram/L (90th percentile of the prostatic group) as the upper limit of "normality," overall sensitivity (stages A-D) for detection of prostatic cancer in 33 essentially untreated patients was 65%. Examples for the followup of therapy of prostatic cancer by measurement of serum PAP with this assay are described.
Clinical experience with a new solid phase enzyme immunoassay for prostatic acid phosphatase
